ID   SCPB_LACLA              Reviewed;         188 AA.
AC   Q9CG34;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Segregation and condensation protein B {ECO:0000255|HAMAP-Rule:MF_01804};
GN   Name=scpB {ECO:0000255|HAMAP-Rule:MF_01804}; OrderedLocusNames=LL1276;
GN   ORFNames=L108430;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Participates in chromosomal partition during cell division.
CC       May act via the formation of a condensin-like complex containing Smc
CC       and ScpA that pull DNA away from mid-cell into both cell halves.
CC       {ECO:0000255|HAMAP-Rule:MF_01804}.
CC   -!- SUBUNIT: Homodimer. Homodimerization may be required to stabilize the
CC       binding of ScpA to the Smc head domains. Component of a cohesin-like
CC       complex composed of ScpA, ScpB and the Smc homodimer, in which ScpA and
CC       ScpB bind to the head domain of Smc. The presence of the three proteins
CC       is required for the association of the complex with DNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01804}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01804}.
CC       Note=Associated with two foci at the outer edges of the nucleoid region
CC       in young cells, and at four foci within both cell halves in older
CC       cells. {ECO:0000255|HAMAP-Rule:MF_01804}.
CC   -!- SIMILARITY: Belongs to the ScpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01804}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK05374.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005176; AAK05374.1; ALT_INIT; Genomic_DNA.
DR   PIR; D86784; D86784.
DR   RefSeq; NP_267432.2; NC_002662.1.
DR   RefSeq; WP_010905863.1; NC_002662.1.
DR   AlphaFoldDB; Q9CG34; -.
DR   SMR; Q9CG34; -.
DR   STRING; 272623.L108430; -.
DR   PaxDb; Q9CG34; -.
DR   EnsemblBacteria; AAK05374; AAK05374; L108430.
DR   KEGG; lla:L108430; -.
DR   PATRIC; fig|272623.7.peg.1379; -.
DR   eggNOG; COG1386; Bacteria.
DR   HOGENOM; CLU_045647_5_3_9; -.
DR   OMA; DGWRFYT; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051304; P:chromosome separation; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 2.
DR   HAMAP; MF_01804; ScpB; 1.
DR   InterPro; IPR005234; ScpB_csome_segregation.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR34298; PTHR34298; 1.
DR   Pfam; PF04079; SMC_ScpB; 1.
DR   PIRSF; PIRSF019345; ScpB; 1.
DR   SUPFAM; SSF46785; SSF46785; 2.
DR   TIGRFAMs; TIGR00281; TIGR00281; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW   Reference proteome.
FT   CHAIN           1..188
FT                   /note="Segregation and condensation protein B"
FT                   /id="PRO_0000211133"
SQ   SEQUENCE   188 AA;  21088 MW;  71BEFA62E636BB6C CRC64;
     MNKTASCELL LFVSGEAGLT LAELSALTEM SKQACQQQID YLKEKYHSDE ESALTIIETA
     GKYRMATKEE FAEILKNYAK TPLNQSLSKS ALEVLSIIAY KQPLTRLEID HLRGVNSSGV
     LSTLRAFDLV EKVGQVEAPG RPSLYATTDF FLDYIGINHL DELPEIDESR FIAEEQTLFN
     ESEENENQ